|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|36545||45136||2005||9 صفحه PDF||سفارش دهید||دانلود رایگان|
The enantioselective hydrolysis of racemic esters and simultaneous separation of the corresponding optically pure (S)-acid as pure isomer is of considerable interest to the pharmaceutical industry as a route to non-steroidal anti-inflammatory drugs. In the present study, an enzymic membrane reactor (EMR) was employed for the optical resolution of racemic ibuprofen ester. EMR consisted of a lipase immobilized polymeric membrane, an organic phase dissolving ester and an aqueous phase to recover the reaction products. The catalytic behaviour of lipase immobilized in a polymeric hollow fibre membrane was investigated using 1-heptyl-ibuprofen ester and 2-ethoxyethyl-ibuprofen ester. The two ester substrates differ in the nature of the alkyl group of the alcohol moiety. The performance of the immobilized enzyme was studied as a function of temperature, pH of phosphate buffer solution and substrate flow rate. The operational conditions that favoured the enzyme selectivity for the (S)-ibuprofen esters, in order to obtain the corresponding (S)-ibuprofen acid as an optically pure single enantiomer, were identified. Lipase from Candida rugosa was used in the hydrolysis of racemic ibuprofen ester. (R)-Ibuprofen ester was found to be less reactive in the reaction. Highest enantioselectivity of enzyme was obtained with phosphate buffer solution of pH 8.0 at temperature of 40 °C and at lower substrate flow rate for both racemic 1-heptyl-ibuprofen and 2-ethoxyethyl-ibuprofen esters. The hydrolysis of racemic 1-heptyl-ibuprofen ester gave 4% eeS, 90% eeP and E value of 1–4, while the hydrolysis of 2-ethoxyethyl-ibuprofen ester resulted in 31% eeS, 85% eeP and E value of 9.5–13 by running the experiment under optimum operating condition in an enzymatic membrane reactor.
Journal: Process Biochemistry - Volume 40, Issue 7, June 2005, Pages 2417–2425